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Database: UniProt
Entry: A0A0K9Y1F3_9FLAO
LinkDB: A0A0K9Y1F3_9FLAO
Original site: A0A0K9Y1F3_9FLAO 
ID   A0A0K9Y1F3_9FLAO        Unreviewed;       298 AA.
AC   A0A0K9Y1F3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=3-hydroxybutyryl-CoA dehydrogenase {ECO:0000313|EMBL:KNB62548.1};
DE            EC=1.1.1.157 {ECO:0000313|EMBL:KNB62548.1};
GN   ORFNames=AC804_06965 {ECO:0000313|EMBL:KNB62548.1};
OS   Chryseobacterium sp. Hurlbut01.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=1681828 {ECO:0000313|EMBL:KNB62548.1, ECO:0000313|Proteomes:UP000036769};
RN   [1] {ECO:0000313|Proteomes:UP000036769}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hurlbut01 {ECO:0000313|Proteomes:UP000036769};
RA   Couger M.B., Youseff N., Elshahed M., French D., Hoff W.;
RT   "Draft Genome Sequence of the Environmental Isolate Chryseobacterium sp.
RT   Hurlbut 01.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) +
CC         NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35;
CC         Evidence={ECO:0000256|ARBA:ARBA00023693};
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000256|ARBA:ARBA00005005}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000256|ARBA:ARBA00004305}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KNB62548.1}.
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DR   EMBL; LGIP01000003; KNB62548.1; -; Genomic_DNA.
DR   RefSeq; WP_050378322.1; NZ_LGIP01000003.1.
DR   AlphaFoldDB; A0A0K9Y1F3; -.
DR   PATRIC; fig|1681828.3.peg.3629; -.
DR   Proteomes; UP000036769; Unassembled WGS sequence.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:RHEA.
DR   GO; GO:0008691; F:3-hydroxybutyryl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0044248; P:cellular catabolic process; IEA:UniProt.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR   GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR022694; 3-OHacyl-CoA_DH.
DR   InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR   InterPro; IPR006108; 3HC_DH_C.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43561; -; 1.
DR   PANTHER; PTHR43561:SF3; HYDROXYACYL-COENZYME A DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00725; 3HCDH; 1.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   PIRSF; PIRSF000105; HCDH; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:KNB62548.1}.
FT   DOMAIN          5..184
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          188..286
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   SITE            141
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-1"
SQ   SEQUENCE   298 AA;  32815 MW;  6DC78584E52933A4 CRC64;
     MNFKNVTVAG SGVLGYQIAF QTAFHGFNVT VYDINDEVLE KAKTKFQILS EAFKKDLGVT
     QEQLDATKIR LSYNSDLAEA VKDADLLIEA VPENPDIKID FYQKLAKLAP EKTVFATNSS
     TLLPSQFAEV TGRPEKFVAL HFANEIWKHN TGEVMRHPHT SDEVFESLLI FAKEIGMVPL
     AIHKEQPGYI VNSLLVPLLG AGLGLLVNGV ADVETIDKTW MVATGAPTGP FGILDVVGIT
     TAYNINKMAA DHTKDPVKQK VVDYLKENFI DKGKLGVATG EGFYTYPDPV YKSKDFLK
//
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